XPO1 binds the beta-catenin:CBY complex

Stable Identifier
R-HSA-3769391
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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CBY1 contains both NLS and NES sequences and continuously shuttles between the cytoplasm and the nucleus. Treatment of cells with leptomycin B (LMB), an inhibitor of XPO1-mediated nuclear export, results in nuclear accumulation of both CBY1 and 14-3-3/YWHAZ proteins (Li et al, 2008; Li et al, 2010). Consistent with this, CBY1 binds to XPO1 in an NES-dependent manner. 14-3-3/YWHAZ enhances the CBY1-XPO1 interaction, possibly by inducing a conformational change that exposes the adjacent NES sequence. Binding of 14-3-3/YWHAZ also inhibits the interaction of CBY1 with alpha-importin, additionally favouring its cytoplasmic localization. CBY1 NES mutants that are incapable of nuclear export show reduced ability to repress a beta-catenin-dependent reporter, and knockdown of endogenous CBY1 causes an accumulation of beta-catenin in the nucleus. These data support a role for CBY1 in the nuclear export of beta-catenin (Li et al, 2010). Despite growing evidence for a role for CBY1 in regulating WNT signaling, a formal requirement for CBY1 in vivo is still lacking.
Literature References
PubMed ID Title Journal Year
19940019 Nuclear-cytoplasmic shuttling of Chibby controls beta-catenin signaling

Hall, J, Mofunanya, A, Fischer, V, Takemaru, K, Li, FQ

Mol. Biol. Cell 2010
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